Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK

The chaperone HYPK regulates the human N-terminal acetyltransferase E (NatE) complex, but the mechanism is not fully understood. Here, the authors study the interplay of NatE and HYPK by cryo-EM and biochemical approaches, providing insights into the molecular basis of N-terminal acetylation of huma...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Sunbin Deng, Nina McTiernan, Xuepeng Wei, Thomas Arnesen, Ronen Marmorstein
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/81657bc1bec14c11ac8cd119b0aa1960
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:81657bc1bec14c11ac8cd119b0aa1960
record_format	dspace
spelling	oai:doaj.org-article:81657bc1bec14c11ac8cd119b0aa19602021-12-02T16:49:15ZMolecular basis for N-terminal acetylation by human NatE and its modulation by HYPK10.1038/s41467-020-14584-72041-1723https://doaj.org/article/81657bc1bec14c11ac8cd119b0aa19602020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14584-7https://doaj.org/toc/2041-1723The chaperone HYPK regulates the human N-terminal acetyltransferase E (NatE) complex, but the mechanism is not fully understood. Here, the authors study the interplay of NatE and HYPK by cryo-EM and biochemical approaches, providing insights into the molecular basis of N-terminal acetylation of human proteins.Sunbin DengNina McTiernanXuepeng WeiThomas ArnesenRonen MarmorsteinNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sunbin Deng Nina McTiernan Xuepeng Wei Thomas Arnesen Ronen Marmorstein Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
description	The chaperone HYPK regulates the human N-terminal acetyltransferase E (NatE) complex, but the mechanism is not fully understood. Here, the authors study the interplay of NatE and HYPK by cryo-EM and biochemical approaches, providing insights into the molecular basis of N-terminal acetylation of human proteins.
format	article
author	Sunbin Deng Nina McTiernan Xuepeng Wei Thomas Arnesen Ronen Marmorstein
author_facet	Sunbin Deng Nina McTiernan Xuepeng Wei Thomas Arnesen Ronen Marmorstein
author_sort	Sunbin Deng
title	Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
title_short	Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
title_full	Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
title_fullStr	Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
title_full_unstemmed	Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
title_sort	molecular basis for n-terminal acetylation by human nate and its modulation by hypk
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/81657bc1bec14c11ac8cd119b0aa1960
work_keys_str_mv	AT sunbindeng molecularbasisfornterminalacetylationbyhumannateanditsmodulationbyhypk AT ninamctiernan molecularbasisfornterminalacetylationbyhumannateanditsmodulationbyhypk AT xuepengwei molecularbasisfornterminalacetylationbyhumannateanditsmodulationbyhypk AT thomasarnesen molecularbasisfornterminalacetylationbyhumannateanditsmodulationbyhypk AT ronenmarmorstein molecularbasisfornterminalacetylationbyhumannateanditsmodulationbyhypk
_version_	1718383405776764928

Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK

Ejemplares similares